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J. Biochem, 1968, Vol. 64, No. 2 197-203
© 1968 Japanese Biochemical Society

research-article

The Purification of Prenyltransferase and Isopentenyl Pyrophosphate Isomerase of Pumpkin Fruit and Their Some Properties

KYOZO OGURA, TOKUZO NISHINO and SHUICHI SETO

From the Chemical Research Institute of Non-Aqueous Solutions, Tohoku University Sendai

Prenyltransferase (farnesyl pyrophosphate synthetase) [EC 2.5.1.1 [EC] ] and isopentenylpyrophosphate isomerase [EG 5.3.3.2 [EC] ] were obtained and partially purified from pumpkin fruit. The prenyltransferase preparation catalyzed the condensation of isopentenyl pyrophosphate with dime-thylallyl pyrophosphate as well as with geranyl pyrophosphate to yield trans-trans farnesyl pyrophosphate as a final product, and was free of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthetase activities. Prenyltransferase of pumpkin has properties similar to those of pig liver, showing requirement of Mg++, Km value of 1.3 × 10–6M for geranyl pyrophosphate, and pH optimum at 7.5.


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